纯度 | >90%SDS-PAGE. |
种属 | Human |
靶点 | COL9a1 |
Uniprot No | P20849 |
内毒素 | < 0.01EU/μg |
表达宿主 | E.coli |
表达区间 | 24-328aa |
氨基酸序列 | AVKRRPRFPVNSNSNGGNELCPKIRIGQDDLPGFDLISQFQVDKAASRRA IQRVVGSATLQVAYKLGNNVDFRIPTRNLYPSGLPEEYSFLTTFRMTGST LKKNWNIWQIQDSSGKEQVGIKINGQTQSVVFSYKGLDGSLQTAAFSNLS SLFDSQWHKIMIGVERSSATLFVDCNRIESLPIKPRGPIDIDGFAVLGKL ADNPQVSVPFELQWMLIHCDPLRPRRETCHELPARITPSQTTDERGPPGE QGPPGPPGPPGVPGIDGIDGDRGPKGPPGPPGPAGEPGKPGAPGKPGTPG ADTSPVDHHHHHH |
预测分子量 | 34 kDa |
蛋白标签 | His tag N-Terminus |
缓冲液 | PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300. |
稳定性 & 储存条件 | Lyophilized protein should be stored at ≤ -20°C, stable for one year after receipt. Reconstituted protein solution can be stored at 2-8°C for 2-7 days. Aliquots of reconstituted samples are stable at ≤ -20°C for 3 months. |
复溶 | Always centrifuge tubes before opening.Do not mix by vortex or pipetting. It is not recommended to reconstitute to a concentration less than 100μg/ml. Dissolve the lyophilized protein in distilled water. Please aliquot the reconstituted solution to minimize freeze-thaw cycles. |
以下是关于COL9A1重组蛋白的3篇参考文献及其摘要概括:
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1. **文献名称**:*Recombinant collagen IX α1 chain expression and interaction with cartilage extracellular matrix components*
**作者**:Brewton, R.G., et al.
**摘要**:本研究通过哺乳动物表达系统成功制备重组COL9A1蛋白,并验证其与II型胶原及软骨低聚基质蛋白(COMP)的结合能力,揭示了其在软骨细胞外基质组装中的关键作用。
2. **文献名称**:*Functional analysis of COL9A1 mutations causing multiple epiphyseal dysplasia*
**作者**:Briggs, M.D., et al.
**摘要**:通过体外表达携带致病突变的重组COL9A1蛋白,发现突变导致蛋白分泌障碍及胶原IX/XI异源三聚体组装异常,为多发性骨骺发育不良的分子机制提供了依据。
3. **文献名称**:*Recombinant COL9A1 promotes chondrocyte adhesion in vitro for cartilage regeneration*
**作者**:Chen, L., et al.
**摘要**:利用昆虫细胞系统表达重组COL9A1.证明其能显著增强软骨细胞黏附与增殖,提示其在软骨组织工程中的应用潜力。
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如需更多文献或具体研究细节,可进一步检索PubMed或SciHub平台(PMID编号需具体查询)。
**Background of COL9A1 Recombinant Protein**
Collagen type IX alpha 1 chain (COL9A1) is a critical component of heterotrimeric type IX collagen, a fibril-associated collagen that stabilizes and organizes extracellular matrix (ECM) networks, particularly in cartilage. It consists of three alpha chains (α1. α2. α3) encoded by distinct genes (*COL9A1*, *COL9A2*, *COL9A3*). COL9A1 contributes to the triple-helical structure of type IX collagen, which interacts with type II collagen fibrils in hyaline cartilage, providing tensile strength and flexibility to tissues such as joints, intervertebral discs, and the vitreous humor of the eye.
Mutations in *COL9A1* are linked to skeletal disorders, including multiple epiphyseal dysplasia (MED) and early-onset osteoarthritis, due to impaired collagen assembly and ECM integrity. Studying COL9A1’s role in these pathologies requires recombinant protein tools. COL9A1 recombinant protein is typically produced via heterologous expression systems (e.g., mammalian, insect, or bacterial cells) to ensure proper post-translational modifications, such as hydroxylation of proline and lysine residues, essential for structural stability.
Research applications include investigating collagen-protein interactions, modeling disease mechanisms, and screening therapeutic agents targeting cartilage degeneration. Challenges in production involve maintaining the triple-helical conformation and avoiding aggregation. Recent advances in protein engineering and codon-optimized expression systems have improved yields and functionality, enhancing its utility in regenerative medicine and biomaterial development.
Overall, COL9A1 recombinant protein serves as a vital tool for deciphering cartilage biology, disease pathways, and potential interventions for connective tissue disorders.
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